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Related Experiment Video

Updated: May 11, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

Protein folding in the endoplasmic reticulum.

Ineke Braakman¹, Daniel N Hebert

¹Cellular Protein Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. i.braakman@uu.nl

Cold Spring Harbor Perspectives in Biology

|May 3, 2013

Summary

This summary is machine-generated.

This article details protein folding within the endoplasmic reticulum (ER), focusing on covalent modifications and resident folding factors. It compares protein folding and exit rates for ER clients.

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Area of Science:

Cell Biology
Biochemistry
Molecular Biology

Background:

Protein folding is crucial for cellular function.
The endoplasmic reticulum (ER) is a key site for protein folding and modification.
Misfolded proteins can lead to cellular dysfunction and disease.

Purpose of the Study:

To provide a comprehensive overview of protein folding in the ER lumen.
To elucidate the roles of specific covalent modifications in protein folding.
To describe the functions of various ER resident folding factors.

Main Methods:

Review of existing literature on ER protein folding.
Analysis of the mechanisms of signal peptide removal, N-linked glycosylation, and disulfide bond formation.
Categorization and functional description of ER folding factors.

Main Results:

Identified three key covalent modifications essential for ER protein folding.
Detailed the involvement of classical chaperones, carbohydrate-binding chaperones, and folding catalysts (PDI, proline cis-trans isomerase).
Compared folding and exit rates of different protein clients within the ER.

Conclusions:

Protein folding in the ER is a complex process involving multiple covalent modifications and a suite of folding factors.
Understanding these processes is vital for comprehending protein homeostasis and disease pathogenesis.
The perspective of the client protein offers insights into ER machinery efficiency.